Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism

Biochemical Journal

Volumn 439, Issue 2, 2011, Pages 215-225

  Wang, Bing ^a,b   Peng, Yingjie ^a,c   Zhang, Tianlong ^a   Ding, Jianping ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Catalytic mechanism; Conformational change; Crystal structure; Kappa class glutathione transferase (GSTk); Kinetic measurement; Substrate binding pocket

Indexed keywords

GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE KAPPA; S HEXYLGLUTATHIONE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; STEADY STATE;

AMINO ACID SEQUENCE; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 80053232321     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110753     Document Type: Article

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